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Literature summary extracted from

  • Yennawar, N.H.; Islam, M.M.; Conway, M.; Wallin, R.; Hutson, S.M.
    Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis (2006), J. Biol. Chem., 281, 39660-39671.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.42 expressed in Escherichia coli BL21 (DE3) cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.42 hanging drop vapour diffusion method using 22-30% polyethlylene glycol 1500, 100 mM HEPES (pH 6.9-7.2), and 20 mM dithiothreitol Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.42 C315A contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity Homo sapiens
2.6.1.42 C315A/C318A contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity Homo sapiens
2.6.1.42 C318A contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.6.1.42 mitochondrion
-
 Homo sapiens 5739
-

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.42 Homo sapiens O15382
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
2.6.1.42 the activity of oxidized BCAT with 0.5 mM hydrogen peroxide for 2 h at 25°C shows 99.5% inhibition Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.42 Ni-NTA acid resin column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.42 L-glutamate + 2-oxoglutarate
-
 Homo sapiens 2-oxoglutarate + L-glutamate
-
 r
2.6.1.42 L-isoleucine + 2-oxoglutarate
-
 Homo sapiens 3-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-leucine + 2-oxoglutarate
-
 Homo sapiens 4-methyl-2-oxopentanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Homo sapiens 3-methyl-2-oxobutanoate + L-glutamate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.6.1.42 BcaT
-
 Homo sapiens
2.6.1.42 branched chain aminotransferase
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.42 50.1
-
 L-glutamate mutant enzyme C315A/C318A Homo sapiens
2.6.1.42 52
-
 L-glutamate mutant enzyme C315A Homo sapiens
2.6.1.42 60.8
-
 L-leucine mutant enzyme C315A/C318A Homo sapiens
2.6.1.42 65
-
 L-leucine mutant enzyme C315A Homo sapiens
2.6.1.42 70.5
-
 L-isoleucine mutant enzyme C315A/C318A Homo sapiens
2.6.1.42 72
-
 L-isoleucine mutant enzyme C315A Homo sapiens
2.6.1.42 188
-
 L-valine mutant enzyme C315A Homo sapiens
2.6.1.42 197
-
 L-valine mutant enzyme C315A/C318A Homo sapiens
2.6.1.42 230
-
 L-valine mutant enzyme C318A Homo sapiens
2.6.1.42 250
-
 2-oxoglutarate mutant enzyme C315A Homo sapiens
2.6.1.42 265
-
 L-glutamate mutant enzyme C318A Homo sapiens
2.6.1.42 270
-
 2-oxoglutarate mutant enzyme C315A/C318A Homo sapiens
2.6.1.42 277
-
 L-valine wild type enzyme Homo sapiens
2.6.1.42 290
-
 L-glutamate wild type enzyme Homo sapiens
2.6.1.42 310
-
 L-leucine mutant enzyme C318A Homo sapiens
2.6.1.42 319
-
 L-isoleucine mutant enzyme C318A Homo sapiens
2.6.1.42 337
-
 L-leucine wild type enzyme Homo sapiens
2.6.1.42 340
-
 2-oxoglutarate wild type enzyme Homo sapiens
2.6.1.42 360
-
 2-oxoglutarate mutant enzyme C318A Homo sapiens
2.6.1.42 371
-
 L-isoleucine wild type enzyme Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.42 pyridoxal 5'-phosphate
-
 Homo sapiens